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MPXV: Update on Morphological and Morphogenesis Aspects Through Transmission and Scanning Electron Microscopies and 3D Reconstruction.
J Med Virol
January 2025
Laboratório de Morfologia e Morfogênese Viral, Instituto Oswaldo Cruz, Fundação Oswaldo Cruz-Fiocruz, Rio de Janeiro, Brazil.
An unprecedented global outbreak caused by the monkeypox virus (MPXV) prompted the World Health Organization to declare a public health emergency of international concern on July 23, 2022. Therapeutics and vaccines for MPXV are not widely available, necessitating further studies, particularly in drug repurposing area. To this end, the standardization of in vitro infection systems is essential.
View Article and Find Full Text PDFMethods to Study Poxvirus Structures by Cryo-EM Imaging Modalities.
Methods Mol Biol
December 2024
Okinawa Institute of Science and Technology Graduate University (OIST), Molecular Cryo-Electron Microscopy Unit, Kunigami, Okinawa, Japan.
Poxviruses are double-stranded DNA viruses that represent the largest known highly pathogenic viruses infecting humans. They undergo dramatic morphological changes during their maturation process, resulting in structural differences between each virion, and their surface is decorated with more than a dozen randomly distributed surface proteins that facilitate viral entry. These are the main reasons poxviruses have eluded high-resolution structure determination.
View Article and Find Full Text PDFCryo-EM structure of orf virus scaffolding protein orfv075.
Biochem Biophys Res Commun
October 2024
School of Pharmacy, Sungkyunkwan University, Suwon, 16419, Republic of Korea. Electronic address:
Article Synopsis
- Capsid-like proteins in poxviruses self-assemble into a lattice that helps form immature virus particles, a key step in virus development.
- The study presents the cryo-electron microscopy structure of the scaffolding protein Orfv075 from orf virus, highlighting conserved regions involved in assembly compared to a related protein in vaccinia virus.
- The research suggests that both viruses have similar assembly mechanisms and identifies the scaffolding protein as a potential target for developing anti-poxvirus treatments.
The palisade layer of the poxvirus core is composed of flexible A10 trimers.
Nat Struct Mol Biol
July 2024
Electron Microscopy of Pathogens, Paul Ehrlich Institute, Langen, Germany.
Due to its asymmetric shape, size and compactness, the structure of the infectious mature virus (MV) of vaccinia virus (VACV), the best-studied poxvirus, remains poorly understood. Instead, subviral particles, in particular membrane-free viral cores, have been studied with cryo-electron microscopy. Here, we compared viral cores obtained by detergent stripping of MVs with cores in the cellular cytoplasm, early in infection.
View Article and Find Full Text PDFMulti-modal cryo-EM reveals trimers of protein A10 to form the palisade layer in poxvirus cores.
Nat Struct Mol Biol
July 2024
Institute of Science and Technology Austria (ISTA), Klosterneuburg, Austria.
Poxviruses are among the largest double-stranded DNA viruses, with members such as variola virus, monkeypox virus and the vaccination strain vaccinia virus (VACV). Knowledge about the structural proteins that form the viral core has remained sparse. While major core proteins have been annotated via indirect experimental evidence, their structures have remained elusive and they could not be assigned to individual core features.
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